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- Publisher
- Wiley
- Copyright
- Copyright © 2005 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309105007761
- pmid
- 16511051
- Publisher site
- See Article on Publisher Site
Abstract
The amino‐acid sequence of cytochrome c552 (PH c552) from a moderately thermophilic bacterium, Hydrogenophilus thermoluteolus, was more than 50% identical to that of cytochrome c from an extreme thermophile, Hydrogenobacter thermophilus (HT c552), and from a mesophile, Pseudomonas aeruginosa (PA c551). The PH c552 gene was overexpressed as a correctly processed holoprotein in the Escherichia coli periplasm. The overexpressed PH c552 has been crystallized by vapour diffusion from polyethylene glycol 4000 pH 6.5. The crystals belong to space group C2221, with unit‐cell parameters a = 48.98, b = 57.99, c = 56.20 Å. The crystals diffract X‐rays to around 2.1 Å resolution.
Journal
Acta Crystallographica Section F – Wiley
Published: Apr 1, 2005